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Literature summary extracted from

  • Voordouw, G.; de Haard, H.; Timmermans, J.A.M.; Veeger, C.; Zabel, P.
    Dissociation and assembly of pyridine nucleotide transhydrogenase from Azotobacter vinelandii (1982), Eur. J. Biochem., 127, 267-274.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.6.1.1 50% inactivation after 10 min in 1 M guanidinium HCl Azotobacter vinelandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.1.1 52000
-
 x * 52000, model of quarternary structure, SDS-PAGE, immunoblot Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
1.6.1.1 Azotobacter vinelandii
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.6.1.1 inactivation by 4 M guanidinium HCl, 4-6% reactivation after transfer in 100 mM Tris buffer, pH 7.5 containing 100 mM FAD Azotobacter vinelandii

Subunits

EC Number Subunits Comment Organism
1.6.1.1 octamer x * 52000, model of quarternary structure, SDS-PAGE, immunoblot Azotobacter vinelandii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.6.1.1 55
-
 approx. 50% activity lost after about 2 min, almost complete loss of activity after 20 min, biphasic inactivation: 70% activity lost with a first-order inactivation constant, 30% is lost much more rapidly, rate of thermal inactivation depends on concentration of NAD+, NADP+, NADH, NADPH, free FAD, Mg2+ and phosphate, independent of pH between pH 5 and pH 9, significant acceleration outside this range, addition of 1 mM FAD lowers inactivation rate about 20fold Azotobacter vinelandii

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.1.1 FAD reduction of FAD leads to its dissociation at enzyme concentrations of 10-100 nM and 30°C-40°C, the apoenzyme can be reactivated to 10-15% by addition of FAD Azotobacter vinelandii